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Journal ArticleDOI

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.

Peter E. Wright, +1 more
- 22 Oct 1999 - 
- Vol. 293, Iss: 2, pp 321-331
TLDR
Many proteins that lack intrinsic globular structure under physiological conditions have now been recognized, and it appears likely that their rapid turnover, aided by their unstructured nature in the unbound state, provides a level of control that allows rapid and accurate responses of the cell to changing environmental conditions.
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This article is published in Journal of Molecular Biology.The article was published on 1999-10-22. It has received 2804 citations till now. The article focuses on the topics: Protein structure function & Intrinsically disordered proteins.

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Citations
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Extended Binding Site on Fibronectin for the Functional Upstream Domain of Protein F1 of Streptococcus pyogenes

TL;DR: Circular dichroism indicated that FUD binds to 70K by β-strand addition, a possibility supported by modeling based on crystal structures of peptides bound to 2F NI-5FNI of the fibrin-binding domain and 8FNI-9F NI of the gelatin- binding domain.
Journal ArticleDOI

Small-Angle X-Ray Scattering- and Nuclear Magnetic Resonance-Derived Conformational Ensemble of the Highly Flexible Antitoxin PaaA2

TL;DR: It is shown that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.
Journal ArticleDOI

Bioinspired single-chain polymer nanoparticles

TL;DR: The 5th International Conference on Biobased and Biodegradable Polymers (ICBP) was held in Donostia-San Sebastian (Spain) del 6 al 9 de octubre de 2015 as mentioned in this paper.
Journal ArticleDOI

Ability of a salivary intrinsically unstructured protein to bind different tannin targets revealed by mass spectrometry

TL;DR: The main role of hydroxyl groups in these interactions and the involvement of hydrogen bonds are demonstrated, in line with sensory analysis, pointing out that the chain length and the level of galloylation are the main factors affecting astringency perception.
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The N0‐binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α‐helices

TL;DR: An isolated peptide corresponding to the 60 first N‐terminal residues of VSV P (P60) and encompassing PNTR has overall molecular dimensions and a dynamic behavior characteristic of a disordered protein but transiently populates conformers containing α‐helices.
References
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The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases

TL;DR: It is demonstrated that p300/CBP acetylates nucleosomes in concert with PCAF, a novel class of acetyltransferases in that it does not have the conserved motif found among various other acetyl transferases.
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The Structural Basis of Estrogen Receptor/Coactivator Recognition and the Antagonism of This Interaction by Tamoxifen

TL;DR: Crystal structures of the human estrogen receptor alpha (hER alpha) ligand-binding domain (LBD) and the OHT-LBD complex reveal the two distinct mechanisms by which structural features of OHT promote this "autoinhibitory" helix 12 conformation.
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Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution

TL;DR: The X-ray crystal structure of a core synaptic fusion complex containing syntaxin-1A, synaptobrevin-II and SNAP-25B reveals a highly twisted and parallel four-helix bundle that differs from the bundles described for the haemagglutinin and HIV/SIV gp41 membrane-fusion proteins.
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Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.

TL;DR: It is argued that the conversion of alpha-helices into beta-sheets underlies the formation of PrPSc, and it is likely that this conformational transition is a fundamental event in the propagation of prions.
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A signature motif in transcriptional co-activators mediates binding to nuclear receptors.

TL;DR: It is proposed that the LXXLL motif is a signature sequence that facilitates the interaction of different proteins with nuclear receptors, and is thus a defining feature of a new family of nuclear proteins.
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